Strucuter and Photochemical Reactions of Photoactive Yellow Proteins: Generality and diversity

2016 Fiscal Year Final Research Report

• Project/Area Number: 24247030
• Research Category: Grant-in-Aid for Scientific Research (A)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Biophysics
• Research Institution: Nara Institute of Science and Technology
• Principal Investigator: Kataoka Mikio 奈良先端科学技術大学院大学, その他, 理事・副学長 (30150254)
• Co-Investigator(Kenkyū-buntansha): 上久保 裕生 奈良先端科学技術大学院大学, 物質創成科学研究科, 准教授 (20311128) ; 山崎 洋一 奈良先端科学技術大学院大学, 物質創成科学研究科, 助教 (40332770)
• Project Period (FY): 2012-04-01 – 2016-03-31
• Keywords: イェロープロテイン / 低障壁水素結合 / 光反応 / 結晶構造解析 / アルギニン / FTIR / キメラ蛋白質 / 国際情報交換

Outline of Final Research Achievements

There are many divergent features even in a structurally homologous proteins. It is not clear how they realize these divergent functions on their same structural backbone. To evaluate these molecular divergent mechanism based on common structure, different PYP proteins have been investigated about their molecular mechanism for their features and functions. From the neutron-X-ray combined crystal analysis and very fast time resolved X-ray crystal analysis, there is a unique low barrier hydrogen bond (LBHB) system as a basic component for PYP features. In this basic system there is a special arginine residue which is deprotonated even in a neutral pH condition. Divergent features on PYP molecules were realized by several residues close or distal site from the LBHB. These residues are located on surface region on PYP molecules.

Free Research Field

生物物理